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小麦蛋白二硫键异构酶通过不同的机制改善面包的特性。

Wheat protein disulfide isomerase improves bread properties via different mechanisms.

机构信息

Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science & Nutritional Engineering, China Agricultural University, 17 East Tsinghua Rd., Beijing 100083, China.

National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, Chaoyang District, Beijing 100101, China.

出版信息

Food Chem. 2020 Jun 15;315:126242. doi: 10.1016/j.foodchem.2020.126242. Epub 2020 Jan 20.

DOI:10.1016/j.foodchem.2020.126242
PMID:31991256
Abstract

Gluten network formation by the oxidation of glutenin sulfhydryl group majorly impacts the subsequent dough and bread properties, and an evolutionary list of chemical oxidants has been used as improvers in bread making. A systematic comparison between azodicarbonamide (ADA), Vc, wheat protein disulfide isomerase (wPDI) and disulfide bond formation protein C (DsbC) of their effects on the alveographic characters of dough and texture properties of subsequent bread was performed. Results show that wPDI improves dough alveographic characters and bread texture properties better in most aspects than other reagents. Free sulfhydryl analysis finds that addition of wPDI increased the free sulfhydryl content in both dough and bread. Compare with inorganic reagents and its bacterial homologue, improving the dough and bread properties with less oxidation of sulfhydryl lead to the proposal that wPDI acts by catalyzing the formation of rheologically active disulfide and reduction of inactive ones in a substrate specific manner.

摘要

谷朊蛋白巯基的氧化形成的面筋网络对面团和面包的后续特性有重大影响,因此化学氧化剂的演变清单被用作面包制作中的改良剂。本文系统比较了偶氮二甲酰胺(ADA)、Vc、小麦蛋白二硫键异构酶(wPDI)和二硫键形成蛋白 C(DsbC)对面团粉质特性和后续面包质地特性的影响。结果表明,在大多数方面,wPDI 对面团粉质特性和面包质地特性的改善作用优于其他试剂。游离巯基分析发现,添加 wPDI 增加了面团和面包中的游离巯基含量。与无机试剂及其细菌同源物相比,用较少的巯基氧化来改善面团和面包的特性,导致 wPDI 通过以底物特异性的方式催化形成流变活性的二硫键和还原非活性二硫键来发挥作用的假设。

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